2016
DOI: 10.1080/10826068.2016.1155059
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Cost-effective and concurrent production of industrially valuable xylano-pectinolytic enzymes by a bacterial isolateBacillus pumilusAJK

Abstract: Simultaneous production of xylanase and pectinase by Bacillus pumilus AJK under submerged fermentation was investigated in this study. Under optimized conditions, it produced 315 ± 16 IU/mL acidic xylanase, 290 ± 20 IU/mL alkaline xylanase, and 88 ± 9 IU/mL pectinase. The production of xylano-pectinolytic enzymes was the highest after inoculating media (containing 2% each of wheat bran and Citrus limetta peel, 0.5% peptone, 10 mM MgSO, pH 7.0) with 2% of 21-hr-old culture and incubated at 37°C for 60 hr at 200… Show more

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Cited by 27 publications
(16 citation statements)
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“… method by measuring the amount of reducing sugars (as xylose equivalent) released during the enzyme–substrate reaction using 3, 5‐dinitrosalicylic acid at optimum enzyme assay pH 8.5 (data not shown) as given by Kaur et al. One unit (IU) of xylanase activity was defined as the amount of enzyme that catalyzed the release of 1 µmol of reducing sugar as xylose equivalent from the substrate in one min under the specified assay conditions.…”
Section: Methodsmentioning
confidence: 99%
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“… method by measuring the amount of reducing sugars (as xylose equivalent) released during the enzyme–substrate reaction using 3, 5‐dinitrosalicylic acid at optimum enzyme assay pH 8.5 (data not shown) as given by Kaur et al. One unit (IU) of xylanase activity was defined as the amount of enzyme that catalyzed the release of 1 µmol of reducing sugar as xylose equivalent from the substrate in one min under the specified assay conditions.…”
Section: Methodsmentioning
confidence: 99%
“…Alkaline pectinase activity was also determined by measuring the release of reducing sugars during the enzyme substrate reaction using Miller's method at optimum enzyme assay pH 9 (data not shown) as given by Kaur et al. . Polymethylgalacturonic acid and polygalacturonic acid (0.5% each) mixture were used as substrates for assaying total pectinase activity.…”
Section: Methodsmentioning
confidence: 99%
“…Enzyme activity was measured according to the method of Miller. 34 Assay conditions were similar to as reported by Kaur et al 24 One IU of enzyme activity is defined as the amount of enzyme that catalyzed the release of 1 μmol of galacturonic acid from polysaccharide (pectin or polygalacturonic acid) in 1 min at temperature 55 C and pH 9.0. 2.7 | Activity of various types of pectinase enzymes 2.7.1 | Exo-polymethylgalacturonase and exopolygalacturonase Miller's method 34 was followed for estimating exo-polymethylgalacturonase (exo-PMG) and exo-polygalacturonase (exo-PG) activity using polymethylgalacturonic acid (1%) and polygalacturonic acid (1%) substrates, respectively.…”
Section: Total Alkaline Pectinase Activitymentioning
confidence: 99%
“…The substrate type mainly decides the commercial viability of the process. Employment of agro‐residues as an alternative carbon source in lieu of commercial xylan or pectin substrates, ensures an economically affordable manufacturing of xylanase and pectinase enzymes . Among various agro‐industrial residues, wheat bran has been mainly reported as a suitable carbon source for the production of xylanase and pectinase enzymes .…”
Section: Introductionmentioning
confidence: 99%
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